纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | DNAJB11 |
Uniprot No | Q9UBS4 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 23-358aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGRDFYKILGVPRSASIKDIKKAYRKLALQ LHPDRNPDDPQAQEKFQDLGAAYEVLSDSEKRKQYDTYGEEGLKDGHQSS HGDIFSHFFGDFGFMFGGTPRQQDRNIPRGSDIIVDLEVTLEEVYAGNFV EVVRNKPVARQAPGKRKCNCRQEMRTTQLGPGRFQMTQEVVCDECPNVKL VNEERTLEVEIEPGVRDGMEYPFIGEGEPHVDGEPGDLRFRIKVVKHPIF ERRGDDLYTNVTISLVESLVGFEMDITHLDGHKVHISRDKITRPGAKLWK KGEGLPNFDNNNIKGSLIITFDVDFPKEQLTEEAREGIKQLLKQGSVQKV YNGLQGY |
预测分子量 | kDa |
蛋白标签 | His tag N-Terminus |
缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于DNAJB11重组蛋白的3篇参考文献示例(注:部分信息为假设性概括,实际文献需通过学术数据库查询确认):
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1. **文献名称**: *DNAJB11 functions as a molecular chaperone in the endoplasmic reticulum*
**作者**: Smith A, et al.
**摘要**: 研究报道DNAJB11作为内质网中的热休克蛋白40家族成员,通过调控未折叠蛋白反应(UPR)协助客户蛋白的正确折叠。重组DNAJB11蛋白实验表明,其与HSP70协同作用,参与错误折叠蛋白的识别与修复。
2. **文献名称**: *DNAJB11 mutations cause autosomal-dominant polycystic kidney disease*
**作者**: Zhang Y, et al.
**摘要**: 该研究通过基因测序发现DNAJB11基因突变与常染色体显性多囊肾病(ADPKD)相关。利用重组突变型DNAJB11蛋白进行功能分析,发现其异常导致内质网应激信号通路激活异常,进而促进囊肿形成。
3. **文献名称**: *Structural insights into DNAJB11’s role in cancer progression*
**作者**: Lee J, et al.
**摘要**: 通过重组DNAJB11蛋白的晶体结构解析,揭示了其J结构域与肿瘤相关蛋白的相互作用机制。实验表明,DNAJB11在多种癌症中高表达,可能通过调控EGFR等信号通路促进肿瘤细胞存活和转移。
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如需具体文献,建议在PubMed或Google Scholar中搜索关键词“DNAJB11 recombinant protein”或结合研究领域筛选近年论文。
DNAJB11. a member of the heat shock protein 40 (Hsp40/DnaJ) family, functions as a co-chaperone for Hsp70 proteins, playing a critical role in regulating protein folding, quality control, and stress response. It is localized primarily in the endoplasmic reticulum (ER) and is involved in the ER-associated degradation (ERAD) pathway, where it assists in recognizing and processing misfolded proteins for proteasomal degradation. Dysregulation of DNAJB11 has been linked to cellular stress conditions, neurodegenerative diseases, and cancer, highlighting its importance in maintaining proteostasis.
Recombinant DNAJB11 protein is engineered through molecular cloning, typically expressed in bacterial (e.g., *E. coli*) or mammalian systems to ensure proper folding and post-translational modifications. The recombinant form retains the conserved J-domain responsible for Hsp70 interaction, along with substrate-binding regions critical for chaperone activity. Its production enables researchers to study DNAJB11’s mechanistic roles in vitro, including its ability to stabilize client proteins, modulate aggregation-prone peptides, and participate in stress granule formation.
Applications of recombinant DNAJB11 span basic research and therapeutic development. It serves as a tool to investigate ER stress responses, protein misfolding disorders (e.g., Alzheimer’s, cystic fibrosis), and cancer biology. Additionally, it is used in drug screening to identify compounds targeting chaperone networks or ERAD components. Recent studies also explore its potential in gene therapy or as a biomarker for diseases linked to proteostatic imbalance. Purification tags (e.g., His-tag) are often incorporated to facilitate isolation and downstream analyses, ensuring high purity and functional integrity for experimental reproducibility.
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